Glucosidase, beta (Bile Acid) 2 (GBA2) ELISA Kits

GBA2 encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Additionally we are shipping GBA2 Antibodies (46) and GBA2 Proteins (5) and many more products for this protein.

list all ELISA KIts Gene Name GeneID UniProt
Anti-Mouse GBA2 GBA2 230101 Q69ZF3
GBA2 298399  
GBA2 57704 Q9HCG7
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Top GBA2 ELISA Kits at antibodies-online.com

Showing 2 out of 3 products:

Catalog No. Reactivity Sensitivity Range Images Quantity Delivery Price Details
Rat 1.875 ng/mL 3.125 ng/mL - 200 ng/mL   96 Tests 11 to 18 Days
$724.89
Details
Human < 0.188 ng/mL 0.313 ng/mL - 20 ng/mL   96 Tests 11 to 18 Days
$838.60
Details

More ELISA Kits for GBA2 Interaction Partners

Zebrafish Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. These results provide a foundation for the use of zebrafish in screening GBA2-targeting molecules, and for wider studies investigating GBA2 biology.

  2. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

Mouse (Murine) Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. results shed light on the molecular mechanism underlying the pathogenesis of GBA2-related hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia (ARCA) and reveal species-specific differences in GBA2 function in vivo

  2. sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity.

  3. GBA2 is particularly abundant in Purkinje cells (PCs), one of the most affected neuronal populations in NPC disease.

  4. glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane. Similar cytoskeletal defects were observed in male germ and Sertoli cells from GBA2 knockout-mice.

  5. the deletion of Gba2 significantly rescues the type 1 Gaucher disease clinical phenotype.

  6. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

  7. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

  8. The repression of IL-6/STAT3 signalling pathway seems to be one of the mechanisms for the delay of liver regeneration in GBA2-deficient mice.

  9. GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples.

  10. The coiled-coil structure of LIMP-2 is required for its interaction with beta-glucocerebrosidase.

  11. L-type calcium channel blockers have the ex vivo effects of increasing GCase activity and protein in mouse fibroblasts

  12. GBA2 is a glucosylceramidase whose loss causes accumulation of glycolipids and an endoplasmic reticulum storage disease

  13. the non-lysosomal glucosylceramidase is identical to the earlier described bile acid beta-glucosidase, being beta-glucosidase 2

  14. testis GBA2 is present in both somatic and germ cells

Human Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. results shed light on the molecular mechanism underlying the pathogenesis of GBA2-related hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia (ARCA) and reveal species-specific differences in GBA2 function in vivo

  2. We conclude that the c.1780G>C mutation results in NLGase loss of function with abolishment of the enzymatic activity and accumulation of GlcCer accompanied by a compensatory increase in GCase.

  3. Demonstrate that GBA2 plays a role in the proinflammatory state characterizing cystic fibrosis cells. Report for the first time that Pseudomonas aeruginosa infection causes a recruitment of plasma membrane-associated glycosphingolipid hydrolases into lipid rafts of CuFi-1-infected cells.

  4. Our protocol showed high specificity and sensitivity for homozygosity detection and facilitated the identification of novel mutations in GAN, GBA2, and ZFYVE26 in four families affected by hereditary spastic paraplegia or Charcot-Marie-Tooth disease

  5. GBA mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology.

  6. GBA2 mutations causing a Marinesco-Sjogren-like syndrome in two Norwegian families, are reported.

  7. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2

  8. sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity.

  9. The results suggested that SPG46 and SPG56 are rare causes of hereditary spastic paraplegia in China.

  10. Spastic paraplegia/cerebellar ataxia patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount.

  11. SPG46 maps to 9p21.2-q21.12 in a Tunisian family with a complicated autosomal recessive hereditary spastic paraplegia with mental impairment and thin corpus callosum

  12. The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis

  13. Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia: GBA2, TGM6, ANO10 and SYT14

  14. We hereby report a novel GBA2 mutation associated with spastic ataxia and suggest that GBA2 mutations may be a relatively frequent cause of autosomal recessive cerebellar ataxias.

  15. observations make GBA2 a likely candidate to be involved in Gaucher disease etiology.

  16. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

  17. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

  18. This study suggests GBA2 mutations are a cause of recessive spastic ataxia and responsible for a form of glucosylceramide storage disease in humans.

  19. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

  20. GBA2 is down-regulated in melanoma; inducible expression of GBA2 affects endogenous sphingolipid metabolism by promoting glucosylceramide degradation (decrease by 78%) and ceramide generation.

GBA2 Antigen Profile

Antigen Summary

This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.

Gene names and symbols associated with GBA2

  • talin 1 (TLN1) antibody
  • glucosidase, beta (bile acid) 2 (gba2) antibody
  • glucosylceramidase beta 2 (GBA2) antibody
  • glucosidase beta 2 (Gba2) antibody
  • glucosylceramidase beta 2 (Gba2) antibody
  • F630034E04 antibody
  • SPG46 antibody
  • TLN1 antibody

Protein level used designations for GBA2

bile acid beta-glucosidase , talin 1 , glucosidase, beta (bile acid) 2 , non-lysosomal glucosylceramidase-like , NLGase , beta-glucocerebrosidase 2 , beta-glucosidase 2 , bile acid , glucosylceramidase 2 , non-lysosomal glucosylceramidase

GENE ID SPECIES
465082 Pan troglodytes
559240 Danio rerio
696062 Macaca mulatta
100145361 Xenopus (Silurana) tropicalis
100438148 Pongo abelii
100476888 Ailuropoda melanoleuca
230101 Mus musculus
298399 Rattus norvegicus
57704 Homo sapiens
100859407 Gallus gallus
474760 Canis lupus familiaris
100155655 Sus scrofa
100139170 Bos taurus
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